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| Isolation, Purification and Compositional Analysis of Antibacterial Peptides from Bovine Bone Collagen |
| ZHANG Shun-liang;PAN Xiao-qian;CHENG Xiao-yu;QIAO Xiao-ling;CHEN Wen-hua;QU Chao;AI Ting |
| China Meat Research Center, Beijing 100068, China |
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Abstract Bovine bone collagen was hydrolyzed by neutral protease, and then the hydrolyate was separated and purified
using ultrafiltration and gel chromatography. The antibacterial peptides obtained were analyzed by reverse high-performance
liquid chromatography (RP-HPLC) and matrix-assisted laser desorption/ionization cascade time of flight mass spectrometry
(MALDI-TOF-TOF-MS). The results showed that the ultrafiltration fractions with molecular weight less than 10 kD had
strong antibacterial activity against Escherichia coli. The peaks I and IV isolated by Sephadex G-25 gel chromatography had
strong antibacterial activity. By RP-HPLC and MALDI-TOF-TOF-MS analysis, the peak I contained a variety of peptides
with molecular weight between 850 and 1550 D, whereas the peak IV contained fewer peptides between 700 and 900 D.
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2013, Vol. 27 
